Electronic and Protein Structural Dynamics of a Photosensory Histidine Kinase

Alexandre, Maxime; Purcell, Erin B.; Grondelle, Rienk van; Robert, Bruno; Kennis, John T. M.; Crosson, Sean

doi:10.1021/bi100527a

Cited by 20 publications

(27 citation statements)

References 57 publications

(90 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, similar to VVD and phototropin the proximal and intermediate conformational responses at the conserved Gln and β-scaffold initiate chemical signaling; however, the distal structural effects differ depending on Ncap or Ccap elements. These variations according to LOV subtype are consistent with the observed variations in the magnitude of structural changes at the β-scaffold (97, 99). Complex structures of light-activated full length proteins and protein complexes ( e.g.…”

Section: Lov Domainssupporting

confidence: 88%

Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein−Protein Interactions

2010

View full text Add to dashboard Cite

Blue light photoreceptors play a pivotal role in detecting the quality and quantity of light in the environment, controlling a wide range of biological responses. Several families of blue-light photoreceptors have been characterized in detail using biophysics and biochemistry, beginning with photon absorption, through intervening signal transduction, to regulation of biological activities. Here we review the Light Oxygen Voltage (LOV), Cryptochrome (CRY) and sensors of Blue Light Using FAD (BLUF) families, three different groups of proteins that offer distinctly different modes of photochemical activation and signal transduction, yet play similar roles in a vast array of biological responses. We cover mechanisms of light activation and propagation of conformational responses that modulate protein:protein interactions involved in biological signaling. Discovery and characterization of these processes in natural proteins are now enabling the design of photoregulatable engineered proteins, facilitating the generation of novel reagents for biochemical and cell biological research.

show abstract

Section: Lov Domainssupporting

confidence: 88%

Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein−Protein Interactions

2010

View full text Add to dashboard Cite

show abstract

“…Although the extent of quaternary rearrangement in this engineered histidine kinase is not established, spectroscopic analysis of the natural LOV histidine kinase, LovK, of Caulobacter crescentus evidences a model in which small changes in overall tertiary/quaternary structure are sufficient to regulate protein activity 100 . Additional structural and biochemical studies are necessary to determine the exact structural mechanism (or mechanisms) by which a LOV domain can regulate histidine kinases.…”

Section: The Discovery Of Lov Domainsmentioning

confidence: 95%

Function, structure and mechanism of bacterial photosensory LOV proteins

2011

Self Cite

View full text Add to dashboard Cite

LOV domains are protein photosensors conserved in bacteria, archaea, plants and fungi that detect blue light via a flavin cofactor. In the bacterial kingdom, LOV domains are present in both chemotrophic and phototrophic species, where they are found N-terminally of signaling and regulatory domains such as sensor histidine kinases, diguanylate cyclases/phosphodiesterases, DNA-binding domains, and σ factor regulators. In this review, we describe the current state of knowledge on the function of bacterial LOV proteins, the structural basis of LOV domain-mediated signal transduction, and the use of LOV domains as genetically-encoded photoswitches in synthetic biology.

show abstract

“…ChpT retains the conserved N-box, which is known to bind a divalent cation (39), but we do not observe electron density consistent with ions or solvent in this region of the structure. Isothermal titration calorimetry (ITC) experiments demonstrate that ChpT, unlike multiple classes of HKs (40,41), is unable to bind ATP (Fig. S4B).…”

Section: B Abortusmentioning

confidence: 99%

Structural asymmetry in a conserved signaling system that regulates division, replication, and virulence of an intracellular pathogen

Willett

Herrou

Briegel

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

We have functionally and structurally defined an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival of the global zoonotic pathogen Brucella abortus. Our study delineates phosphoryl transfer through this molecular pathway, which initiates from the sensor kinase CckA and proceeds through the ChpT phosphotransferase to two regulatory substrates: CtrA and CpdR. Genetic perturbation of this system results in defects in cell growth and division site selection, and a specific viability deficit inside human phagocytic cells. Thus, proper control of B. abortus division site polarity is necessary for survival in the intracellular niche. We further define the structural foundations of signaling from the central phosphotransferase, ChpT, to its response regulator substrate, CtrA, and provide evidence that there are at least two modes of interaction between ChpT and CtrA, only one of which is competent to catalyze phosphoryltransfer. The structure and dynamics of the active site on each side of the ChpT homodimer are distinct, supporting a model in which quaternary structure of the 2:2 ChpT-CtrA complex enforces an asymmetric mechanism of phosphoryl transfer between ChpT and CtrA. Our study provides mechanistic understanding, from the cellular to the atomic scale, of a conserved transcriptional regulatory system that controls the cellular and infection biology of B. abortus. More generally, our results provide insight into the structural basis of two-component signal transduction, which is broadly conserved in bacteria, plants, and fungi.rucellosis, caused by Brucella spp., is among the most common zoonotic diseases worldwide (1). These intracellular pathogens are estimated to cause at least 500,000 new human infections each year and, in areas of Africa, Asia, and South America, inflict significant agricultural losses due to decreased livestock production (2, 3). Survival of Brucella within mammals is linked to their ability to infect and survive inside professional phagocytic cells (2). If left untreated in human hosts, Brucella eventually spread to multiple tissue types, which can lead to a range of debilitating chronic sequelae including reticuloendothelial, cardiovascular, gastrointestinal, and neurological damage.Brucella are members of the α-proteobacteria, a diverse class of Gram-negative species adapted for growth across a range of environmental conditions including plant surfaces and roots, aquatic and soil ecosystems, and the interior of mammalian cells (4, 5). Among the central regulatory systems controlling the α-proteobacterial cell cycle is a multistep phosphorelay composed of four proteins: (i) the hybrid sensor histidine kinase (HK) CckA, (ii) the histidine phosphotransferase ChpT, (iii) the DNA-binding response regulator CtrA, and (iv) the phospho-receiver protein CpdR (Fig. 1). Our current understanding of this conserved regulatory system is based largely on studies of the related aquatic bacterium Caulobacter crescentus (6, 7). In Ca...

show abstract

Electronic and Protein Structural Dynamics of a Photosensory Histidine Kinase

Cited by 20 publications

References 57 publications

Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein−Protein Interactions

Tripping the Light Fantastic: Blue-Light Photoreceptors as Examples of Environmentally Modulated Protein−Protein Interactions

Function, structure and mechanism of bacterial photosensory LOV proteins

Structural asymmetry in a conserved signaling system that regulates division, replication, and virulence of an intracellular pathogen

Contact Info

Product

Resources

About